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PDBsum entry 5jyh

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protein links
Toxin PDB id
5jyh

 

 

 

 

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Contents
Protein chain
44 a.a.
PDB id:
5jyh
Name: Toxin
Title: Solution structure of hge36: scorpine-like peptide from hadrurus gertschi
Structure: Hge-scorpine. Chain: a. Synonym: hg-scorpine-like 1,hgscplike1. Engineered: yes
Source: Hadrurus gertschi. Scorpion. Organism_taxid: 380989. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: D.Flores-Solis,R.Rodriguez De La Vega,F.Del Rio-Portilla
Key ref: D.Flores-Solis et al. (2016). Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi. Febs Lett, 590, 2286-2296. PubMed id: 27314815 DOI: 10.1002/1873-3468.12255
Date:
13-May-16     Release date:   29-Jun-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q0GY40  (KBX3_HOFGE) -  Hge-scorpine from Hoffmannihadrurus gertschi
Seq:
Struc:
95 a.a.
44 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1002/1873-3468.12255 Febs Lett 590:2286-2296 (2016)
PubMed id: 27314815  
 
 
Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi.
D.Flores-Solis, Y.Toledano, O.Rodríguez-Lima, P.Cano-Sánchez, B.E.Ramírez-Cordero, A.Landa, R.C.Rodríguez de la Vega, F.Del Rio-Portilla.
 
  ABSTRACT  
 
Scorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channel-blocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold.
 

 

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